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Database: UniProt
Entry: A0A402A3X2_9CHLR
LinkDB: A0A402A3X2_9CHLR
Original site: A0A402A3X2_9CHLR 
ID   A0A402A3X2_9CHLR        Unreviewed;       438 AA.
AC   A0A402A3X2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:GCE13858.1};
GN   ORFNames=KTT_37170 {ECO:0000313|EMBL:GCE13858.1};
OS   Tengunoibacter tsumagoiensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Tengunoibacter.
OX   NCBI_TaxID=2014871 {ECO:0000313|EMBL:GCE13858.1, ECO:0000313|Proteomes:UP000287352};
RN   [1] {ECO:0000313|Proteomes:UP000287352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno3 {ECO:0000313|Proteomes:UP000287352};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU361152};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCE13858.1}.
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DR   EMBL; BIFR01000001; GCE13858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402A3X2; -.
DR   Proteomes; UP000287352; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW   Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287352}.
FT   DOMAIN          193..406
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            108
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   438 AA;  47284 MW;  1B4102BEB30C2A3C CRC64;
     MKERIVLIGA GSAVFTRGLV ADLITRGVET ELVLVDSDPE ALAAAEKLTA KMIASRQAPI
     QLSASVDRRT VLAGATVVIC TIGVGGRRAW EQDVFIPRKY GIIVPVGDTV GPGGSSRALR
     MIPAMIAIAQ DVLDLAPEAL FFNYGNPMAP VCRAIHKATG AKVIGLCHGV NAVAAYLSRA
     LRVPQADLHY TAVGINHLTW FTALRVNGQD ALPRLHEIAA ERLLDPYEGE PFSWRLFELF
     HAFPAVLDRH VTEFFPQFFR EGAYYGGKTL GNEAFSFEDT IAGGDETFEQ MRTDALAAEP
     LPTDYFERIG GEHEQVLEIV EAIRTERGTI FSANLPNTGQ VPNLPREVIV ESPAVADGSG
     LHALALPALP AALVGTLATR YMWAETIVEA ALEGSRTKFI QALVLDGSVK SLEMASSVAD
     ELLEAQAAYL PWVKREGL
//
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